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Cobalt Toxicity and Human Health
Published in Debasis Bagchi, Manashi Bagchi, Metal Toxicology Handbook, 2020
Md. Hafiz Uddin, Marufa Rumman
Genetic background plays a role in Co-NPs toxicity. A study was also performed with long-term exposures of 12 weeks to sub-toxic doses (0.05 mg/mL) of Co-NPs to assess the oxidative DNA damage. Ogg1 deleted mouse embryonic fibroblast (MEF) failed to remove the 8-OH-dG lesions from DNA. Consequently, MEF accumulates ROS, cellular transformation, increases in metalloproteinases (MMPs), and anchorage-independent growth suggested potential cancer risk associated with Ogg1 genetic background. The study observed increase in expressions of antioxidant genes (Figure 15.1), Gstp1, Sod2, Ho1, and Keap1 in Ogg1 deleted MEF, which can be mediated by the activation of nuclear factor erythroid-2-related factor-2 (Nrf2). The conditioned media from MEF Ogg1 deleted cells promote the growth of HeLa cells. This further confirms that MEF Ogg1 deleted cells are prone to acquire oncogenic characteristics [13].
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Published in Chad A. Mirkin, Spherical Nucleic Acids, 2020
William E. Briley, Madison H. Bondy, Pratik S. Randeria, Torin J. Dupper, Chad A. Mirkin
Conventional Nanoflares do not allow one to determine the spatial distribution of RNA within the cell. Indeed, Nanoflare-transcript binding results in a displacement of the fluorophore-labeled sequence from the nanoparticle construct, which spatially separates the fluorescent reporter and transcript (Fig. 101.1, upper). However, with a simple design change where the flare sequence is made longer and complementary to the target RNA transcript, a new construct can be realized that can track and quantify RNA within a cell (Fig. 101.1, lower). Herein, we report the synthesis and development of such a construct, termed the Sticky-flare, and investigate its use as a platform for RNA quantification and real-time tracking of transcripts as they are transported within live HeLa and mouse embryonic fibroblast (MEF) cells. These constructs and their activity in cells represent the only way of measuring both the quantity and location of mRNA in live cells.
Embryonic Stem Cells
Published in Richard K. Burt, Alberto M. Marmont, Stem Cell Therapy for Autoimmune Disease, 2019
Dan S. Kaufman, James A. Thomson
Recently, the culture conditions required for growth of undifferentiated human ES cells have been refined. Whereas the original derivation of these cells used irradiated mouse embryonic fibroblast (MEF) feeder cells and media containing fetal bovine serum, it is now possible to grow these cells in serum-free media and on plates coated with either Matrigel® or laminin.25 Growth without feeder cells still requires “conditioned media” taken from cultures of MEFs. The requirement for “conditioned media” suggests that soluble factor(s) produced by the MEFs are essential for maintenance of undifferentiated ES cell growth. These refinements in the culture methods are the start of a process to identify the conditions that are essential for maintenance of human ES cell self-renewal. Eventually, use of a chemically defined media will aide in large-scale growth of human ES cells as a prelude to better cell-based therapies.
Anticancer activity of vanadium nanoparticles against human breast cancer: an in vitro study
Published in Inorganic and Nano-Metal Chemistry, 2023
Canan Vejselova Sezer, Hatice Mehtap Kutlu
The anticancer effect of vanadium has been investigated in many malignant cell lines, with their biochemical and molecular mechanisms. These cell lines are B- and T-cell lymphoma, hepatoma, osteosarcoma, testicular, breast, uterine, kidney, lung, nasopharynx, and esophageal carcinoma cells.[11,12] Researchers have shown the antitumor effect of (+4) sodium metavanadate and (+4) vanadyl sulfate as vanadium compounds in many in vitro studies on lymphoma, T-cell leukemia, erythroleukemia, basophilic leukemia, liver cancer, ovarian cancer, testicular cancer, and cancers of esophagus and bone.[6,13,14] It has also been demonstrated that vanadium (NaVO3) inhibits cancer cell viability in human lung (A549) and breast cancer (A549) cells.[5] The cytotoxic and antitumor effects of vanadyl sulfate and bis malato orthovanadium on mouse fibrosarcoma cells (L929), rat pheochromocytoma cells (PC12), human liver carcinoma cells (HepG2) and mouse embryonic fibroblast cells (NIH/3T3) were investigated in various studies. It was found that its cytotoxic effect on 3T3 cells was lower than its cytotoxic effect on other tested cancer cells, and that this cytotoxicity varied depending on the dose and cell type.[15]
Selective adsorption of bilirubin against albumin to alkylamine functionalized PVA microspheres
Published in Journal of Biomaterials Science, Polymer Edition, 2019
Yingda Ma, Jian Chen, Jian Li, Wenyan Han, Yamin Chai, Tingting Wang, Qian Zhang, Lichun Wang, Weichao Wang, Zhexiang Wang, Lailiang Ou
The cytotoxicity of adsorbents was evaluated by the extraction method [34,35]. Four grams of adsorbent was immersed in 20 ml culture media of DMEM, containing 10% fetal bovine serum (FBS), and the extract liquid was obtained after incubation at 37 °C for 72 h. Highly differentiated NIH 3T3 mouse embryonic fibroblast cells were cultured in complete DMEM media at 37 °C in an atmosphere of 5% CO2. For cell viability assays, cells were plated in 96-well plates at a density of 1 × 103 cells per well and maintained for 24 h. To evaluate the cytotoxicity of adsorbents, the culture media in 96-well plates was replaced by: (a) 250 μL complete DMEM media as a negative control; (b) 250 μL culture media of 95% complete DMEM and 5% DMSO as a positive control; (c) 250 μL extract liquid as experimental groups. The cells were then incubated for 72 h, and the cell viability was determined by the thiazolyl-blue-tetrazolium-bromide (MTT) assay. Briefly, 20 μL of stock MTT (5 mg/mL) mixed with 100 μL of DMEM medium was added into the 96-well plate, and the plate was incubated at 37 °C. Four hours later, 150 μL of DMSO was added after the medium-MTT solution was removed. Finally, the absorbance intensity at 570 nm was measured with an ELISA reader. At least three independent experiments with five replicates were carried out.
Nonviral gene delivery using PAMAM dendrimer conjugated with the nuclear localization signal peptide derived from human papillomavirus type 11 E2 protein
Published in Journal of Biomaterials Science, Polymer Edition, 2021
Jeil Lee, Yong-Eun Kwon, Jaegi Kim, Dong Woon Kim, Hwanuk Guim, Jehyeong Yeon, Jin-Cheol Kim, Joon Sig Choi
Neuro-2A mouse neuroblastoma cells and mouse embryonic fibroblast cells (NIH3T3) were grown in medium containing 89% DMEM, 10% FBS, and 1% antibiotic-antimycotic reagent. All cell lines were maintained in 100-mm cell culture dishes (Corning) at 37 ○С in a humidified atmosphere (5% CO2/95% air). Both cell lines were cultured in 96-well plates at a density of 1.8 × 104 cells/well and incubated for 16 h to obtain 70–80% confluency prior to the addition of polyplexes. Polyplexes were prepared by mixing pCN-Luci (0.5 μg) with PEI 25 kDa, Lipofectamine 2000, PAMAM G2, RKRAR-PAMAM G2, and RKRARH-PAMAM G2 at multiple weight ratios and incubated for 30 min. Lipofectamine 2000 was used according to the manufacturer’s protocol (1:1, v/v). The N/P ratios of each polyplex at the 1:1 weight ratio (polymer:DNA) were 7.7, 1.6, 1.9, and 1.6 for PEI 25 kDa, PAMAM G2, RKRAR-PAMAM G2, and RKRARH-PAMAM G2, respectively (Table S2). Once the cells reached 70–80% confluency, the polyplex solution was added and cells were incubated for 24 h at 37°С. Cells were washed with Dulbecco’s phosphate buffered saline (DPBS) and treated with a reporter lysis buffer (Promega, Seoul, South Korea). Plates were incubated for 30 min at room temperature and the resulting lysates were harvested into microcentrifuge tubes and centrifuged at 13,200 rpm for 10 min. Luciferase activities of the lysates were analyzed using a Lumat LB 9507 instrument (Berthold Technology, Bad Wildbad, Germany); protein concentrations were measured using a Micro BCATM protein assay kit. Finally, luciferase activity was calculated as relative light units (RLU) per microgram of total protein.